Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
Deciphering the mechanism of protein folding is one of the most desirable goals in the field of structural biology. Apart from the structural information about the native state, in-depth knowledge about the conformational properties of the unfolded and intermediate states of proteins is important to...
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| Format: | Theses and Dissertations |
| Language: | English |
| Published: |
2014
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| Online Access: | http://hdl.handle.net/10356/60568 |
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| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | Deciphering the mechanism of protein folding is one of the most desirable goals in the field of structural biology. Apart from the structural information about the native state, in-depth knowledge about the conformational properties of the unfolded and intermediate states of proteins is important to understand the folding process. This information can further provide insight into the events of protein misfolding and aggregation that result in variety of diseases. |
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